Q7M757 (BRC3L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lys-63-specific deubiquitinase BRCC36-like
EC=3.4.19.-

Gene names

Name:	C6.1al
Synonyms:	Gm5136

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains By similarity.
Sequence similarities	Belongs to the peptidase M67A family. BRCC36 subfamily. Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G2/M transition DNA damage checkpoint Inferred from sequence or structural similarity. Source: UniProtKB double-strand break repair Inferred from sequence or structural similarity. Source: UniProtKB histone H2A K63-linked deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of DNA repair Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to ionizing radiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	BRCA1-A complex Inferred from sequence or structural similarity. Source: UniProtKB BRISC complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB polyubiquitin binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 291	291	Lys-63-specific deubiquitinase BRCC36-like		PRO_0000373951
Regions
	Motif	122 – 135	14	JAMM motif
Sites
	Metal binding	122	1	Zinc; catalytic By similarity
	Metal binding	124	1	Zinc; catalytic By similarity
	Metal binding	135	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7M757 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: F45CC0496EDC0130	FASTA	291	33,079
	10 20 30 40 50 60 MAVRMMQGVQ AVYLESDAFL VCLNHALSTE KEEVMGLCIG QLNDHGRSDS RLAYAGAEMC 70 80 90 100 110 120 TVAKKMEATR IVHIHSVIIL RRSDKTKDRV EISPEQLSAA SIEAERLAEQ TGRPMRVVGW 130 140 150 160 170 180 YHSHPHITVW PSHVDVRTQA MYQMMDQSFV GLIFACFIED KPTKIGRVLY TCFQSVQASK 190 200 210 220 230 240 SSEYERLEIP IHIVPRTTIG TVCLRSAIEL PGILCQEEQE AYRRIHGLTH LDSVTKIHNG 250 260 270 280 290 SVFTKHLCSQ MSAVCGPLLQ WLEDRLEQNQ QRLQELEQEK EDLMEELSSL E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 135-291. Strain: C57BL/6J. Tissue: Olfactory bulb.
[3]	"Human and mouse proteases: a comparative genomic approach." Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C. Nat. Rev. Genet. 4:544-558(2003) [PubMed: 12838346] [Abstract] Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC120506 mRNA. Translation: AAI20507.1. BC120508 mRNA. Translation: AAI20509.1. AK134982 mRNA. Translation: BAE22368.1. BN000130 mRNA. Translation: CAD67592.1.
IPI	IPI00279112.
RefSeq	NP_988991.1. NM_203660.2.
UniGene	Mm.452758.
3D structure databases
ProteinModelPortal	Q7M757.
ModBase	Search...
Protein family/group databases
MEROPS	M67.007.
Proteomic databases
PRIDE	Q7M757.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	368203.
KEGG	mmu:368203.
UCSC	uc007gzj.2. mouse.
Organism-specific databases
MGI	MGI:3647286. Gm5136.
Gene expression databases
Genevestigator	Q7M757.
Family and domain databases
InterPro	IPR000555. Mov34_MPN_PAD1. [Graphical view]
KO	K11864.
Pfam	PF01398. Mov34. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	400944.
SOURCE	Search...

Entry information

Entry name

BRC3L_MOUSE

Accession

Primary (citable) accession number: Q7M757
Secondary accession number(s): Q3UY45

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	December 15, 2003
Last modified:	November 16, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program